Kallikrein-2 (KLK2) is a secreted serine protease that belongs to the peptidase S1 family of Kallikrein subfamily. KLK2 contains 1 peptidase S1 domain. It is highly expressed in the human prostate gland. KLK2 can cleave Met-Lys and Arg-Ser bonds in kininogen to release Lys-bradykinin, but Preferential cleavages of Arg-|-Xaa bonds in small molecule substrates. It also highly selective action to release kallidin (lysyl-bradykinin) from kininogen involves hydrolysis of Met-|-Xaa or Leu-|-Xaa. KLK2 is inhibited by serpins such as protein C inhibitor, antichymotrypsin, and plasminogen. KLK2 is considered to be a biomarker for prostate cancer.
KLK3(Kallikrein 3), also known as Prostate Specific Antigen (PSA), kallikrein-related peptidase 3, Gamma-seminoprotein, is a secreted protein of the glandular kallikrein subfamily of serine proteases.KLK3 contains one peptidase S1 domain.KLK3 is a glycoprotein produced almost exclusively by the prostate gland. Growing evidence suggests that many kallikreins are implicated in carcinogenesis and some have potential as novel cancer and other disease biomarkers.
Human Kallikrein 7 is a member of the tissue kallikrein family of extracellular serine proteases that is made up of 15 members. It is predominantly expressed in the skin. A major physiological function of Kallikrein 7 is to regulate the desquamation process (the shedding of corneocytes from the outer layer of the epidermis) through proteolysis of the intercellular adhesive structures between corneocytes. Dysregulation of Kallikrein 7 has been linked to several inflammatory skin diseases including atopic dermatitis, psoriasis, and Netherton syndrome. Studies have shown that Kallikrein 5 is a potential physiological activator for Kallikrein 7. The proform of Kallikrein 7 can be activated by thermolysin.
Kallikrein-8, also known as Neuropsin, Serine protease 19, Serine protease TADG-14, Tumor-associated differentially expressed gene 14 protein and KLK8, is a secreted protein which belongs to thepeptidase S1 family and Kallikrein subfamily. It is a serine protease which is capable of degrading a number of proteins such as casein, fibrinogen, kininogen, fibronectin and collagen type IV. Kallikrein-8 / KLK8 plays a role in the formation and maturation of orphan and small synaptic boutons in the Schaffer-collateral pathway. It regulates Schaffer-collateral long-term potentiation in the hippocampus and is required for memory acquisition and synaptic plasticity. It is involved in skin desquamation and keratinocyte proliferation and plays a role in the secondary phase of pathogenesis following spinal cord injury. It also cleaves L1CAM in response to increased neural activity. It induces neurite outgrowth and fasciculation of cultured hippocampal neurons. Kallikrein-8 / KLK8 is expressed at high levels in serum, ascites fluid and tumor cytosol of advanced stage ovarian cancer patients and may serve as a marker of ovarian cancer. Kallikrein-8 / KLK8 may have potential clinical value for disease diagnosis or prognosis and it may also be a useful therapeutic target.
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